Monocot chimeric jacalins: a novel subfamily of plant lectins

Ma, Qing‐Hu

doi:10.3109/07388551.2013.793650

Cited by 19 publications

(21 citation statements)

References 52 publications

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“…Although lectins from plants and other species have been an important topic of research for years, most studies dealt with the identification and expansion of a particular lectin family in one species, or specifically focused on one type of lectin motif and its distribution in the plant kingdom [27,28,29,30,31,32,33,34,35,36]. To date, there have only been a few publications that report on the distribution of multiple lectin motifs across plant species.…”

Section: Introductionmentioning

confidence: 99%

Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics

Holle

Schutter

Eggermont

et al. 2017

IJMS

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Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant lectin domains identified in five representative core angiosperm genomes (Arabidopsis thaliana, Glycine max, Cucumis sativus, Oryza sativa ssp. japonica and Oryza sativa ssp. indica). The genomes were screened for genes encoding lectin domains using a combination of Basic Local Alignment Search Tool (BLAST), hidden Markov models, and InterProScan analysis. Additionally, phylogenetic relationships were investigated by constructing maximum likelihood phylogenetic trees. The results demonstrate that the majority of the lectin families are present in each of the species under study. Domain organization analysis showed that most identified proteins are multi-domain proteins, owing to the modular rearrangement of protein domains during evolution. Most of these multi-domain proteins are widespread, while others display a lineage-specific distribution. Furthermore, the phylogenetic analyses reveal that some lectin families evolved to be similar to the phylogeny of the plant species, while others share a closer evolutionary history based on the corresponding protein domain architecture. Our results yield insights into the evolutionary relationships and functional divergence of plant lectins.

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Section: Introductionmentioning

confidence: 99%

Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics

Holle

Schutter

Eggermont

et al. 2017

IJMS

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“…In the past few years many jacalin-related lectin genes have been associated with disease resistance, abiotic stress signaling, wounding, insect damage, or multiple stresses (Song et al 2014). Structural analyses indicated that Hfr-1 and Ta-JA1 share similar three-dimensional structures with other jacalin-related proteins, such as wheat vernalization-related gene 2 (Ver2), wheat chemically induced gene-1(WCI-1), and maize beta-glucosidase-aggregating factor (BGAF) (Ma 2014). …”

Section: Jacalin-like Proteins With Dirigent Domainmentioning

confidence: 99%

“…In contrast the mannose-specific lectins are synthesized without a signal peptide and accumulate in the nucleocytoplasmic compartment of the plant cell. Many mannosespecific jacalin-related domains are linked to a disease response or dirigent domain, thus forming another group of AB-type proteins (Ma 2014). All proteins of this type reported so far have exclusively been found in the Poaceae family.…”

Section: Jacalin-like Proteins With Dirigent Domainmentioning

confidence: 99%

“…Especially in wheat, almost half of the jacalin-like proteins contain a dirigent domain (Song et al 2014). It was hypothesized that these chimeric proteins may have evolved from jacalin-related lectins by fusion with a dirigent domain at the N-terminus, which could broaden the physiological role of jacalin-related lectins (Ma 2014).…”

Section: Jacalin-like Proteins With Dirigent Domainmentioning

confidence: 99%

“…Overexpression of the jacalin-related domain alone in tobacco plants conferred the same resistance to P. syringe similar to the whole protein while overexpression of the dirigent domain resulted in altered sensitivity of wheat seedlings to salts. It was suggested that the jacalin-related domain of Ta-JA1 provides a basic disease resistance whereas the dirigent domain plays a role in fine-tuning the activity of Ta-JA1 (Ma 2014). In the past few years many jacalin-related lectin genes have been associated with disease resistance, abiotic stress signaling, wounding, insect damage, or multiple stresses (Song et al 2014).…”

Section: Jacalin-like Proteins With Dirigent Domainmentioning

confidence: 99%

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Plant AB Toxins with Lectin Domains

Shang¹,

Dang²,

Damme³

2015

Plant Toxins

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As part of their defense system different plant species each express a diverse set of defense proteins, among them proteins with lectin domains. The whole group of plant lectins assembles all proteins that have the ability to recognize and bind specific carbohydrate structures. Based on the sequence and the conformation of the carbohydrate recognition domains several lectin families are distinguished. Although many lectins are composed only of carbohydrate binding domains, several lectins are chimeric proteins composed of a lectin domain and another unrelated domain. In some cases this second domain can be considered as a toxin domain. This chapter focuses on different types of plant AB toxins and their physiological importance in the battle against pathogens and predators. Most information is available on type 2 ribosome-inactivating proteins in which an N-glycosidase domain is linked through a disulfide bridge to a lectin domain. More recently chimeric proteins consisting of one or more lectin domains and a dirigent domain or aerolysin domain have also been discovered. Although these AB toxins all consist of a lectin domain and a toxin domain, the nature of the toxin and the lectin domain are different resulting in proteins with different carbohydrate binding properties as well as a different mode of action for toxicity.

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